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Published online before print March 30, 2007, 10.1110/ps.072820907
Protein Science (2007), 16:977-982. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of HI1506, a novel two-domain protein from Haemophilus influenzae

Nese Sari1, Yanan He1, Victoria Doseeva1, Karen Surabian1, Jayanthi Ramprakash1, Fred Schwarz2, Osnat Herzberg1, and John Orban1

1 Center for Advanced Research in Biotechnology, University of Maryland Biotechnology Institute, Rockville, Maryland 20850, USA
2 National Institute of Standards and Technology, Rockville, Maryland 20850, USA

(RECEIVED February 13, 2007; FINAL REVISION February 13, 2007; ACCEPTED February 14, 2007)

HI1506 is a 128-residue hypothetical protein of unknown function from Haemophilus influenzae. It was originally annotated as a shorter 85-residue protein, but a more detailed sequence analysis conducted in our laboratory revealed that the full-length protein has an additional 43 residues on the C terminus, corresponding with a region initially ascribed to HI1507. As part of a larger effort to understand the functions of hypothetical proteins from Gram-negative bacteria, and H. influenzae in particular, we report here the three-dimensional solution NMR structure for the corrected full-length HI1506 protein. The structure consists of two well-defined domains, an {alpha}/beta 50-residue N-domain and a 3-{alpha} 32-residue C-domain, separated by an unstructured 30-residue linker. Both domains have positively charged surface patches and weak structural homology with folds that are associated with RNA binding, suggesting a possible functional role in binding distal nucleic acid sites.

Keywords: structural genomics; NMR; Haemophilus influenzae; hypothetical protein


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